{"metadata":{"accession":"IPR001313","entry_id":null,"type":"repeat","go_terms":[{"identifier":"GO:0003723","name":"RNA binding","category":{"code":"F","name":"molecular_function"}}],"source_database":"interpro","member_databases":{"pfam":{"PF22493":"NOP9-like PUF repeat domain","PF00806":"Pumilio-family RNA binding repeat"},"profile":{"PS50302":"Pumilio RNA-binding repeat profile"},"smart":{"SM00025":"Pumilio-like repeats"}},"integrated":null,"hierarchy":{"accession":"IPR001313","name":"Pumilio RNA-binding repeat","type":"Repeat","children":[]},"name":{"name":"Pumilio RNA-binding repeat","short":"Pumilio_RNA-bd_rpt"},"description":[{"text":"<p>Members of the Pumilio family of proteins (Puf) regulate translation and mRNA stability in a wide variety of eukaryotic organisms including mammals, flies, worms, slime mold, and yeast [[cite:PUB00018238]]. Pumilio family members are characterised by the presence of eight tandem copies of an imperfectly repeated 36 amino acids sequence motif, the Pumilio repeat, surrounded by a short N- and C-terminal conserved region. The eight repeats and the N- and C-terminal regions form the Pumilio homology domain (PUM-HD). The PUM-HD domain is a sequence-specific RNA binding domain. The Puf family of proteins are mainly post-transcriptional regulators. Several Puf members have been shown to bind specific RNA sequences mainly found in the 3' UTR of mRNA and repress their translation [[cite:PUB00018239], [cite:PUB00094378]]. Frequently, Puf proteins function asymmetrically to create protein gradients, thus causing asymmetric cell division and regulating cell fate specification [[cite:PUB00018240]].</p>\n\n<p>Crystal structure of Pumilio repeats has been solved [[cite:PUB00018241]]. The PUM repeat with the N- and C-terminal regions pack together to form a right-handed superhelix that approximates a half doughnut structurally similar to the Armadillo (ARM) repeat proteins, beta-catenin and\nkaryopherin alpha. The RNA binds the concave surface of the molecule, where\neach of the protein's eight repeats makes contacts with a different RNA base\nvia three amino acid side chains at conserved positions [[cite:PUB00018242]].</p>\n\n<p>This entry represents the Pumilio repeat.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00018238":{"PMID":10662662,"ISBN":null,"volume":"10","issue":"2","year":2000,"title":"Translational repression: a duet of Nanos and Pumilio.","URL":null,"raw_pages":"R81-3","medline_journal":"Curr Biol","ISO_journal":"Curr. Biol.","authors":["Parisi M","Lin H."],"DOI_URL":"http://dx.doi.org/10.1016/S0960-9822(00)00283-9"},"PUB00018239":{"PMID":14584586,"ISBN":null,"volume":"55","issue":"7","year":2003,"title":"The PUF family of RNA-binding proteins: does evolutionarily conserved structure equal conserved function?","URL":null,"raw_pages":"359-66","medline_journal":"IUBMB Life","ISO_journal":"IUBMB Life","authors":["Spassov DS","Jurecic R."],"DOI_URL":"http://dx.doi.org/10.1080/15216540310001603093"},"PUB00018242":{"PMID":12202039,"ISBN":null,"volume":"110","issue":"4","year":2002,"title":"Modular recognition of RNA by a human pumilio-homology domain.","URL":null,"raw_pages":"501-12","medline_journal":"Cell","ISO_journal":"Cell","authors":["Wang X","McLachlan J","Zamore PD","Hall TM."],"DOI_URL":"http://dx.doi.org/10.1016/S0092-8674(02)00873-5"},"PUB00018240":{"PMID":1459455,"ISBN":null,"volume":"6","issue":"12A","year":1992,"title":"Pumilio is essential for function but not for distribution of the Drosophila abdominal determinant Nanos.","URL":null,"raw_pages":"2312-26","medline_journal":"Genes Dev","ISO_journal":"Genes Dev.","authors":["Barker DD","Wang C","Moore J","Dickinson LK","Lehmann R."],"DOI_URL":"http://www.genesdev.org/cgi/content/abstract/6/12A/2312"},"PUB00018241":{"PMID":11336708,"ISBN":null,"volume":"7","issue":"4","year":2001,"title":"Crystal structure of a Pumilio homology domain.","URL":null,"raw_pages":"855-65","medline_journal":"Mol Cell","ISO_journal":"Mol. Cell","authors":["Wang X","Zamore PD","Hall TM."],"DOI_URL":"http://dx.doi.org/10.1016/S1097-2765(01)00229-5"},"PUB00094378":{"PMID":29385744,"ISBN":null,"volume":"19","issue":"2","year":2018,"title":"The PUF Protein Family: Overview on PUF RNA Targets, Biological Functions, and Post Transcriptional Regulation.","URL":null,"raw_pages":null,"medline_journal":"Int J Mol Sci","ISO_journal":"Int J Mol Sci","authors":["Wang M","Oge L","Perez-Garcia MD","Hamama L","Sakr S."],"DOI_URL":null},"PUB00050752":{"PMID":18328718,"ISBN":null,"volume":"16","issue":"4","year":2008,"title":"Structures of human Pumilio with noncognate RNAs reveal molecular mechanisms for binding promiscuity.","URL":null,"raw_pages":"549-57","medline_journal":"Structure","ISO_journal":"Structure","authors":["Gupta YK","Nair DT","Wharton RP","Aggarwal AK."],"DOI_URL":"http://dx.doi.org/10.1016/j.str.2008.01.006"},"PUB00050806":{"PMID":18327269,"ISBN":null,"volume":"15","issue":"4","year":2008,"title":"Basis of altered RNA-binding specificity by PUF proteins revealed by crystal structures of yeast Puf4p.","URL":null,"raw_pages":"397-402","medline_journal":"Nat Struct Mol Biol","ISO_journal":"Nat. Struct. Mol. Biol.","authors":["Miller MT","Higgin JJ","Hall TM."],"DOI_URL":"http://dx.doi.org/10.1038/nsmb.1390"},"PUB00052211":{"PMID":19540345,"ISBN":null,"volume":null,"issue":null,"year":2009,"title":"Structure and RNA binding of the mouse Pumilio-2 Puf Domain.","URL":null,"raw_pages":null,"medline_journal":"J Struct Biol","ISO_journal":"J. Struct. Biol.","authors":["Jenkins HT","Baker-Wilding R","Edwards TA."],"DOI_URL":null},"PUB00057141":{"PMID":21653694,"ISBN":null,"volume":"286","issue":"30","year":2011,"title":"Specific and modular binding code for cytosine recognition in Pumilio/FBF (PUF) RNA-binding domains.","URL":null,"raw_pages":"26732-42","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Dong S","Wang Y","Cassidy-Amstutz C","Lu G","Bigler R","Jezyk MR","Li C","Hall TM","Wang Z."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M111.244889"}},"set_info":null,"overlaps_with":[{"accession":"IPR011989","name":"Armadillo-like helical","type":"homologous_superfamily"},{"accession":"IPR016024","name":"Armadillo-type fold","type":"homologous_superfamily"}],"counters":{"subfamilies":0,"domain_architectures":551,"interactions":1,"matches":194208,"pathways":4,"proteins":34346,"proteomes":3602,"sets":0,"structural_models":{"alphafold":29405,"bfvd":0},"structures":78,"taxa":10282},"entry_annotations":{"alignment:seed":120,"alignment:full":3592},"cross_references":{"prositedoc":{"displayName":"PROSITE Doc","description":"PROSITE is a database of protein families and domains.","rank":18,"accessions":[{"accession":"PDOC50302","url":"http://prosite.expasy.org/PDOC50302"}]}},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"5kla","name":"Crystal structure of the drosophila Pumilio RNA-binding domain in complex with hunchback RNA"}}}